GDIR1_RAT
ID GDIR1_RAT Reviewed; 204 AA.
AC Q5XI73;
DT 02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-NOV-2004, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Rho GDP-dissociation inhibitor 1 {ECO:0000250|UniProtKB:P19803};
DE Short=Rho GDI 1 {ECO:0000250|UniProtKB:P19803};
DE AltName: Full=Rho-GDI alpha {ECO:0000250|UniProtKB:P19803};
GN Name=Arhgdia {ECO:0000312|RGD:1359547};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1] {ECO:0000312|EMBL:AAH83817.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Brown Norway {ECO:0000269|PubMed:15489334};
RC TISSUE=Kidney {ECO:0000312|EMBL:AAH83817.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=19343716; DOI=10.1002/pmic.200800664;
RA Maurya D.K., Sundaram C.S., Bhargava P.;
RT "Proteome profile of the mature rat olfactory bulb.";
RL Proteomics 9:2593-2599(2009).
RN [3]
RP FUNCTION, AND INTERACTION WITH PLXNB3 AND RAC1.
RX PubMed=20696765; DOI=10.1074/jbc.m110.120451;
RA Li X., Lee A.Y.;
RT "Semaphorin 5A and plexin-B3 inhibit human glioma cell motility through
RT RhoGDIalpha-mediated inactivation of Rac1 GTPase.";
RL J. Biol. Chem. 285:32436-32445(2010).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34 AND SER-47, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [5]
RP INTERACTION WITH KANK2.
RX PubMed=25961457; DOI=10.1172/jci79504;
RA Gee H.Y., Zhang F., Ashraf S., Kohl S., Sadowski C.E., Vega-Warner V.,
RA Zhou W., Lovric S., Fang H., Nettleton M., Zhu J.Y., Hoefele J.,
RA Weber L.T., Podracka L., Boor A., Fehrenbach H., Innis J.W., Washburn J.,
RA Levy S., Lifton R.P., Otto E.A., Han Z., Hildebrandt F.;
RT "KANK deficiency leads to podocyte dysfunction and nephrotic syndrome.";
RL J. Clin. Invest. 125:2375-2384(2015).
CC -!- FUNCTION: Controls Rho proteins homeostasis. Regulates the GDP/GTP
CC exchange reaction of the Rho proteins by inhibiting the dissociation of
CC GDP from them, and the subsequent binding of GTP to them. Retains Rho
CC proteins such as CDC42, RAC1 and RHOA in an inactive cytosolic pool,
CC regulating their stability and protecting them from degradation.
CC Actively involved in the recycling and distribution of activated Rho
CC GTPases in the cell, mediates extraction from membranes of both
CC inactive and activated molecules due its exceptionally high affinity
CC for prenylated forms. Through the modulation of Rho proteins, may play
CC a role in cell motility regulation. In glioma cells, inhibits cell
CC migration and invasion by mediating the signals of SEMA5A and PLXNB3
CC that lead to inactivation of RAC1. {ECO:0000250|UniProtKB:P52565,
CC ECO:0000250|UniProtKB:Q99PT1, ECO:0000269|PubMed:20696765}.
CC -!- SUBUNIT: Monomer (By similarity). Interacts with FER (By similarity).
CC Interacts with PLXNB3 (PubMed:20696765). Forms a heterodimer with RAC1
CC (PubMed:20696765). Interacts with RHOA, the affinity is increased by
CC three orders of magnitude when RHOA is prenylated (By similarity).
CC Interacts with PSMD10; the interaction increases ARHGDIA association
CC with RHOA, leading to ARHGDIA-mediated inactivation of RHOA and ROCK
CC and prolonged AKT activation (By similarity). Interacts with KANK2; the
CC interaction is direct and may regulate the interaction of ARHGDIA with
CC RHOA, RAC1 and CDC42 (PubMed:25961457). Interacts with RHOC (By
CC similarity). Interacts with CDC42 (By similarity). Interacts with NGFR
CC (via death domain); NGFR binding decreases the affinity for RHOA (By
CC similarity). {ECO:0000250|UniProtKB:P52565,
CC ECO:0000250|UniProtKB:Q99PT1, ECO:0000269|PubMed:20696765,
CC ECO:0000269|PubMed:25961457}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19343716}.
CC -!- SIMILARITY: Belongs to the Rho GDI family. {ECO:0000255}.
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DR EMBL; BC083817; AAH83817.1; -; mRNA.
DR RefSeq; NP_001007006.1; NM_001007005.1.
DR RefSeq; XP_006247959.1; XM_006247897.3.
DR RefSeq; XP_006247960.1; XM_006247898.2.
DR AlphaFoldDB; Q5XI73; -.
DR SMR; Q5XI73; -.
DR BioGRID; 262122; 3.
DR IntAct; Q5XI73; 7.
DR MINT; Q5XI73; -.
DR STRING; 10116.ENSRNOP00000051840; -.
DR iPTMnet; Q5XI73; -.
DR PhosphoSitePlus; Q5XI73; -.
DR SwissPalm; Q5XI73; -.
DR World-2DPAGE; 0004:Q5XI73; -.
DR jPOST; Q5XI73; -.
DR PaxDb; Q5XI73; -.
DR PRIDE; Q5XI73; -.
DR Ensembl; ENSRNOT00000114464; ENSRNOP00000080561; ENSRNOG00000036688.
DR GeneID; 360678; -.
DR KEGG; rno:360678; -.
DR CTD; 396; -.
DR RGD; 1359547; Arhgdia.
DR eggNOG; KOG3205; Eukaryota.
DR GeneTree; ENSGT00390000006233; -.
DR HOGENOM; CLU_076228_1_1_1; -.
DR InParanoid; Q5XI73; -.
DR OMA; DDDKRCH; -.
DR OrthoDB; 1265661at2759; -.
DR PhylomeDB; Q5XI73; -.
DR TreeFam; TF105387; -.
DR Reactome; R-RNO-193634; Axonal growth inhibition (RHOA activation).
DR Reactome; R-RNO-209563; Axonal growth stimulation.
DR Reactome; R-RNO-8980692; RHOA GTPase cycle.
DR Reactome; R-RNO-9013106; RHOC GTPase cycle.
DR Reactome; R-RNO-9013148; CDC42 GTPase cycle.
DR Reactome; R-RNO-9013149; RAC1 GTPase cycle.
DR Reactome; R-RNO-9013404; RAC2 GTPase cycle.
DR Reactome; R-RNO-9013407; RHOH GTPase cycle.
DR Reactome; R-RNO-9013408; RHOG GTPase cycle.
DR PRO; PR:Q5XI73; -.
DR Proteomes; UP000002494; Chromosome 10.
DR Bgee; ENSRNOG00000036688; Expressed in spleen and 19 other tissues.
DR Genevisible; Q5XI73; RN.
DR GO; GO:0005829; C:cytosol; IDA:RGD.
DR GO; GO:0005615; C:extracellular space; IDA:RGD.
DR GO; GO:0001772; C:immunological synapse; ISO:RGD.
DR GO; GO:0016020; C:membrane; IDA:RGD.
DR GO; GO:0005634; C:nucleus; ISO:RGD.
DR GO; GO:0045202; C:synapse; IDA:SynGO.
DR GO; GO:0005504; F:fatty acid binding; IDA:RGD.
DR GO; GO:0005096; F:GTPase activator activity; IEA:UniProtKB-KW.
DR GO; GO:0051879; F:Hsp90 protein binding; IDA:RGD.
DR GO; GO:0019901; F:protein kinase binding; IDA:RGD.
DR GO; GO:0005094; F:Rho GDP-dissociation inhibitor activity; ISO:RGD.
DR GO; GO:0031267; F:small GTPase binding; IPI:RGD.
DR GO; GO:0071260; P:cellular response to mechanical stimulus; IMP:RGD.
DR GO; GO:0071407; P:cellular response to organic cyclic compound; IEP:RGD.
DR GO; GO:0071461; P:cellular response to redox state; IEP:RGD.
DR GO; GO:0030336; P:negative regulation of cell migration; IMP:UniProtKB.
DR GO; GO:2000249; P:regulation of actin cytoskeleton reorganization; ISO:RGD.
DR GO; GO:0008360; P:regulation of cell shape; IMP:RGD.
DR GO; GO:0032880; P:regulation of protein localization; ISO:RGD.
DR GO; GO:0035023; P:regulation of Rho protein signal transduction; ISO:RGD.
DR GO; GO:0007266; P:Rho protein signal transduction; ISO:RGD.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR Gene3D; 2.70.50.30; -; 1.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR000406; Rho_GDI.
DR InterPro; IPR024792; RhoGDI_dom_sf.
DR PANTHER; PTHR10980; PTHR10980; 1.
DR Pfam; PF02115; Rho_GDI; 1.
DR PRINTS; PR00492; RHOGDI.
DR SUPFAM; SSF81296; SSF81296; 1.
PE 1: Evidence at protein level;
KW Acetylation; Cytoplasm; GTPase activation; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CHAIN 2..204
FT /note="Rho GDP-dissociation inhibitor 1"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT /id="PRO_0000349124"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 43
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q99PT1"
FT MOD_RES 47
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 105
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 127
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 141
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT MOD_RES 141
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q99PT1"
FT MOD_RES 178
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 138
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
FT CROSSLNK 141
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:P52565"
SQ SEQUENCE 204 AA; 23407 MW; 8ACE6F4456D842D8 CRC64;
MAEQEPTAEQ LAQIAAENEE DEHSVNYKPP AQKSIQEIQE LDKDDESLRK YKEALLGRVA
VSADPNVPNV IVTRLTLVCS TAPGPLELDL TGDLESFKKQ SFVLKEGVEY RIKISFRVNR
EIVSGMKYIQ HTYRKGVKID KTDYMVGSYG PRAEEYEFLT PMEEAPKGML ARGSYNIKSR
FTDDDKTDHL SWEWNLTIKK EWKD
